Piezo1 trimer passively transports cations across the plasma membrane according to their concentration gradients

Stable Identifier
R-MMU-9855091
Type
Reaction [transition]
Species
Mus musculus
Compartment
cytosol, plasma membrane, extracellular region
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Piezo1 trimer passively transports cations across the plasma membrane according to their concentration gradients
Piezo1 is a non-selective cation channel that passively transports Ca2+, K+, Mg2+, and Na+ across the plasma membrane in response to mechanical force on the membrane (Coste et al. 2010, Cox et al. 2016, Wang et al. 2018, Zeng et al. 2022). Piezo1 forms trimers with a central channel and three blades that protrude in the plane of the membrane (Ge et al. 2015, Mulhall et al. 2023). The Piezo1 trimer is not flat in the plane of the membrane but rather forms a dome (Lin et al. 2019, Mulhall et al. 2023). Application of force to the membrane opens the central channel of the Piezo1 trimer, likely through lateral tension on the membrane that deforms the Piezo1 dome (Lewis and Grandl 2015, Lin et al. 2019, Yang et al. 2022). Piezo1 colocalizes with Gja1 (Connexin 43 channels) in the plasma membrane of osteocytes and the colocalization increases with stimulation of Piezo1 by force (Zeng et al. 2022).
Literature References
PubMed ID Title Journal Year
26785635 Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension

Cox, CD, Bae, C, Ziegler, L, Hartley, S, Nikolova-Krstevski, V, Rohde, PR, Ng, CA, Sachs, F, Gottlieb, PA, Martinac, B

Nat Commun 2016
36457052 Mechanosensitive piezo1 calcium channel activates connexin 43 hemichannels through PI3K signaling pathway in bone

Zeng, Y, Riquelme, MA, Hua, R, Zhang, J, Acosta, FM, Gu, S, Jiang, JX

Cell Biosci 2022
31435018 Force-induced conformational changes in PIEZO1

Lin, YC, Guo, YR, Miyagi, A, Levring, J, Mackinnon, R, Scheuring, S

Nature 2019
29610524 A lever-like transduction pathway for long-distance chemical- and mechano-gating of the mechanosensitive Piezo1 channel

Wang, Y, Chi, S, Guo, H, Li, G, Wang, L, Zhao, Q, Rao, Y, Zu, L, He, W, Xiao, B

Nat Commun 2018
26390154 Architecture of the mammalian mechanosensitive Piezo1 channel

Ge, J, Li, W, Zhao, Q, Li, N, Chen, M, Zhi, P, Li, R, Gao, N, Xiao, B, Yang, M

Nature 2015
20813920 Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels

Coste, B, Mathur, J, Schmidt, M, Earley, TJ, Ranade, S, Petrus, MJ, Dubin, AE, Patapoutian, A

Science 2010
35388220 Structure deformation and curvature sensing of PIEZO1 in lipid membranes

Yang, X, Lin, C, Chen, X, Li, S, Li, X, Xiao, B

Nature 2022
37587339 Direct observation of the conformational states of PIEZO1

Mulhall, EM, Gharpure, A, Lee, RM, Dubin, AE, Aaron, JS, Marshall, KL, Spencer, KR, Reiche, MA, Henderson, SC, Chew, TL, Patapoutian, A

Nature 2023
26646186 Mechanical sensitivity of Piezo1 ion channels can be tuned by cellular membrane tension

Lewis, AH, Grandl, J

Elife 2015
Participants
Input
Output
Catalyst Activity

mechanosensitive monoatomic cation channel activity of Piezo1 trimer [plasma membrane]

Physical Entity
Piezo1 trimer [plasma membrane] (Mus musculus)
Activity
mechanosensitive monoatomic cation channel activity (GO:0140135)
Orthologous Events
PIEZO1 trimer passively transports cations across the plasma membrane according to their electrochemical gradients (Homo sapiens)
Authored
May, B  (2023-11-29)
Reviewed
Xiao, R  (2024-07-16)
Farach-Carson, MC  (2024-10-27)
Wu, D  (2024-10-27)
Created
May, B  (2023-11-29)
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